PNC-27 | Buy Research-Grade PNC-27 in Europe | ≥99% Purity

PNC-27 is a synthetic chimeric peptide comprising an N-terminal MDM2-binding domain derived from the p53 transactivation domain fused to a C-terminal penetratin cell-penetrating peptide sequence, designed as a selective cancer cell membrane-disrupting agent that targets HDM2 (MDM2) expressed at the plasma membrane surface of tumour cells, available to buy in Europe for laboratory research into cancer cell selective cytotoxicity, p53/MDM2 interaction biology, tumour cell membrane HDM2 biology, membrane-active anticancer peptide pharmacology, and the comparative study of p53-derived chimeric anticancer peptides.

Laboratories and research institutions across the EU can order verified, research-grade PNC-27 with fast international dispatch to Europe, full batch documentation, and ≥99% purity confirmed by HPLC and Mass Spectrometry.

✅ ≥99% Purity — HPLC & Mass Spectrometry Verified

✅ Batch-Specific Certificate of Analysis (CoA)

✅ Sterile Lyophilised Powder | GMP Manufactured

✅ Fast Dispatch to EU & Europe | Tracked Shipping

What is PNC-27?

PNC-27 is a 32-amino acid synthetic chimeric peptide developed by Bowne, Michl, and colleagues, constructed by fusing two functional domains: an N-terminal sequence (residues 1–16 of PNC-27) derived from the p53 transactivation domain (p53 residues 12–26) that encodes the MDM2-binding helix of p53, and a C-terminal penetratin sequence (residues 17–32) derived from the Antennapedia homeodomain — one of the most widely characterised arginine/lysine-rich cell-penetrating peptide (CPP) sequences that facilitates membrane translocation of peptide cargoes. The resulting chimeric peptide combines the MDM2-binding pharmacophore of the p53 transactivation domain with the membrane-active, cell-penetrating properties of penetratin — producing a molecule whose cancer cell selectivity derives from a mechanism fundamentally distinct from classical intracellular p53/MDM2 interaction disruption.

The central and mechanistically defining feature of PNC-27’s biology — distinguishing it from other p53/MDM2 interaction disruptors including Nutlin-3a, RG7112, and stapled p53 peptides — is that its cytotoxic activity against cancer cells operates at the plasma membrane level rather than through intracellular nuclear MDM2 inhibition. Studies characterising PNC-27’s mechanism established that HDM2 (the human MDM2 homologue) is expressed at the surface of tumour cell plasma membranes — a localisation not present in normal non-transformed cells — and that PNC-27 binds this membrane-resident HDM2 through its p53 transactivation domain sequence, with the penetratin component then driving membrane disruption through pore formation and membranolytic activity. The result is selective necrotic cell death of HDM2 membrane-expressing cancer cells, while normal cells — lacking surface HDM2 — are spared from PNC-27’s membranolytic activity.

This membrane-level HDM2-targeted mechanism has several mechanistic consequences that distinguish PNC-27 from intracellular MDM2 inhibitors. PNC-27’s cytotoxicity is p53-status independent — active against both p53 wild-type and p53-null cancer cells — because the mechanism does not require intracellular p53 release or p53-dependent transcriptional apoptosis, but instead produces direct membrane disruption in any cell expressing surface HDM2. Cancer cells are killed through necrosis rather than apoptosis — with rapid membrane permeabilisation, organelle swelling, and necrotic morphology rather than the caspase-dependent chromatin condensation of apoptotic death. And the selectivity determinant is surface HDM2 expression — a tumour-associated membrane phenotype rather than a specific genetic mutation — making PNC-27 broadly active across cancer cell types expressing membrane HDM2 regardless of their p53 mutational status or intracellular signalling background.

What Does PNC-27 Do in Research?

In laboratory settings, PNC-27 is studied across cancer cell selective cytotoxicity, membrane HDM2 biology, p53 transactivation domain pharmacology, membrane-active anticancer peptide mechanisms, necrotic versus apoptotic cell death pathways, and comparative p53/MDM2 research. EU and European researchers working with PNC-27 typically focus on:

Cancer cell selective membrane disruption and HDM2 surface biology — The most mechanistically distinctive research application of PNC-27 is as a probe for surface HDM2 expression in cancer cells — binding membrane-resident HDM2 through the p53 transactivation domain sequence and producing selective membranolytic cytotoxicity in HDM2-expressing tumour cells while sparing normal cells. Studies use PNC-27 to examine surface HDM2 expression across cancer cell lines and primary tumour cells, characterise the distribution and density of membrane HDM2 as a tumour-associated surface antigen, and establish the correlation between surface HDM2 expression level and PNC-27 cytotoxic sensitivity — using surface biotinylation, flow cytometry, and proximity ligation assays to quantify membrane HDM2 and correlate it with PNC-27 cell killing efficiency.

p53/MDM2 interaction domain pharmacology — PNC-27’s N-terminal sequence is derived from the p53 transactivation domain helix that inserts into the hydrophobic cleft of MDM2 — the same interaction surface targeted by small molecule MDM2 inhibitors including Nutlin-3a and RG7112. Studies use PNC-27 as a peptide-based p53/MDM2 interaction probe — examining its binding to recombinant MDM2, characterising the structural determinants of p53 transactivation domain/MDM2 interaction through PNC-27 alanine scanning variants, and establishing the binding affinity and interaction kinetics of the PNC-27 MDM2-binding sequence compared to the parent p53 peptide and small molecule MDM2 inhibitors. These p53/MDM2 interaction pharmacology studies provide mechanistic context for the membrane HDM2-targeting specificity of PNC-27.

Necrotic cell death mechanism research — PNC-27 kills cancer cells through necrosis — rapid, ATP-independent membrane disruption producing organelle swelling, lysosomal rupture, and cellular contents release — rather than the caspase-dependent apoptosis pathway engaged by most conventional anticancer agents. Studies use PNC-27 to examine the necrotic cell death programme — characterising plasma membrane permeabilisation kinetics (propidium iodide uptake, LDH release, HMGB1 secretion), organelle morphology changes, the absence of caspase activation, and the ATP-independence of PNC-27-driven cell death — establishing the necrotic death signature in cancer cells treated with PNC-27 and distinguishing it from apoptotic cell death driven by intracellular MDM2 inhibitors and DNA-damaging agents.

p53-independent cancer cell killing research — A critical research property of PNC-27 — distinguishing it from all intracellular p53/MDM2 pathway-targeted agents — is its activity against p53-null and p53-mutant cancer cells. Since PNC-27’s mechanism requires surface HDM2 binding and membrane disruption rather than intracellular p53 release and p53-dependent transcription, its cytotoxicity is entirely independent of p53 expression, mutation status, and transcriptional activity. Studies use PNC-27 in p53 wild-type, p53-null (p53 knockout), and p53 hotspot mutant isogenic cancer cell pairs to establish p53-independence — demonstrating equivalent PNC-27 cytotoxicity regardless of p53 status and establishing surface HDM2 expression as the sole determinant of PNC-27 sensitivity.

Membrane pore formation and membranolytic mechanism research — PNC-27’s penetratin C-terminal sequence is a cationic arginine-rich cell-penetrating peptide that at sufficient local membrane concentrations — achieved when PNC-27 accumulates at the cancer cell surface through HDM2-mediated tethering — drives membrane destabilisation and pore formation through electrostatic interaction with negatively charged lipid head groups and hydrophobic membrane insertion. Studies examine the biophysical mechanism of PNC-27 membranolytic activity — using model membrane systems (liposomes, supported lipid bilayers), dye leakage assays, atomic force microscopy, and electron microscopy of PNC-27-treated cancer cell membranes — to characterise the membrane pore morphology, the kinetics of membrane permeabilisation, and the concentration dependence of membranolytic activity relative to HDM2-binding-dependent local peptide accumulation.

Comparative p53/MDM2 pathway intervention research — PNC-27 is systematically studied alongside Nutlin-3a (MDM2 E3 ligase/p53 interaction inhibitor acting intracellularly), RG7112, AMG-232, and stapled p53 peptides (ATSP-7041) in comparative studies that characterise the mechanistic differences between intracellular nuclear MDM2 inhibition and membrane-level surface HDM2 targeting. These comparative studies examine differences in p53 dependency, cell death modality (apoptosis versus necrosis), activity in p53-mutant cancers, and the relationship between MDM2 localisation (nuclear/cytoplasmic versus membrane) and susceptibility to each class of MDM2-targeted agent — establishing PNC-27 as a mechanistically distinct complement to intracellular MDM2 inhibitors in the p53/MDM2 research toolkit.

Cancer cell line HDM2 surface expression profiling research — The selectivity of PNC-27 for surface HDM2-expressing cancer cells makes it a research tool for profiling HDM2 surface expression across tumour cell populations — characterising which cancer types, cell lines, and primary tumour cells express HDM2 at the plasma membrane and in what density. Studies use PNC-27 cytotoxicity, biotinylated PNC-27 surface binding, and direct surface HDM2 immunostaining to map the distribution of surface HDM2 expression across panels of cancer cell lines from different histological origins — establishing which cancer types are likely PNC-27 sensitive and characterising the relationship between surface HDM2 density and PNC-27 potency.

Pancreatic cancer and drug-resistant cancer biology — PNC-27 has been studied in pancreatic cancer — a cancer type characterised by frequent p53 mutations, KRAS-driven signalling, and profound resistance to conventional chemotherapy — where its p53-independent, surface HDM2-targeted mechanism provides a rationale for activity in a cancer type where p53-dependent apoptosis pathways are functionally compromised. Studies use PNC-27 in pancreatic cancer cell lines and gemcitabine-resistant sublines to examine PNC-27 cytotoxicity, surface HDM2 expression, and the activity of PNC-27 in combination with conventional chemotherapy — characterising PNC-27’s potential as a mechanistic complement to DNA-damaging agents that lose efficacy in p53-null or p53-mutant settings.

Melanoma and solid tumour biology research — Early characterisation studies documented PNC-27 activity in melanoma cell lines alongside normal melanocytes — establishing the cancer cell selectivity principle in a cell system where normal and transformed counterparts could be directly compared in matched conditions. Studies in melanoma and other solid tumour systems use PNC-27 to examine the differential surface HDM2 expression between tumour and normal cell pairs, characterise the morphological features of PNC-27-driven necrotic cell death in solid tumour cells, and establish the concentration range producing selective tumour cell killing without normal cell toxicity.

PNC-28 and chimeric peptide structure-activity relationship research — PNC-28 is a related chimeric peptide sharing the penetratin C-terminal sequence of PNC-27 but incorporating a different N-terminal p53 transactivation domain sequence — providing a direct comparator for examining the contribution of specific p53 domain residues to MDM2 binding affinity, surface HDM2 targeting efficiency, and cancer cell cytotoxic potency. Studies comparing PNC-27 and PNC-28 in matched cell systems characterise the structure-activity relationship within the p53 transactivation domain/penetratin chimeric peptide series — establishing which p53 residues are critical for membrane HDM2 engagement and which contribute to potency differences between the two family members.

Tumour microenvironment and immune cell interaction research — PNC-27’s necrotic cell death mechanism releases damage-associated molecular patterns (DAMPs) — including HMGB1, calreticulin, and ATP — that activate innate immune responses and promote dendritic cell maturation and antigen cross-presentation. Studies examining PNC-27-driven immunogenic cell death characterise DAMP release profiles from PNC-27-treated cancer cells, examine the downstream activation of macrophages and dendritic cells by PNC-27-conditioned necrotic cell supernatants, and probe whether PNC-27-induced necrosis promotes anti-tumour immune responses through DAMP-mediated innate immune activation — establishing a potential immunological dimension to PNC-27’s cancer cell killing biology.

Cell-penetrating peptide biology and membrane translocation research — The penetratin C-terminal domain of PNC-27 is one of the most extensively studied cell-penetrating peptide sequences in the CPP literature — with its membrane translocation mechanism debated between direct membrane permeation and endocytic uptake pathways. Studies examining PNC-27 membrane interactions characterise the contribution of penetratin’s arginine-rich sequence to PNC-27’s membranolytic activity in the context of surface HDM2-mediated local concentration — probing whether HDM2 binding-dependent accumulation of PNC-27 at the cancer cell surface shifts the penetratin translocation mechanism toward membrane disruption rather than endocytosis-dependent cellular entry observed at sub-membranolytic concentrations.

All research applications are for in vitro and pre-clinical use only.

What Do Studies Say About PNC-27?

PNC-27 has a focused but mechanistically important research literature — anchored in the characterisation studies by Bowne, Michl, Weiner and colleagues that established the surface HDM2 mechanism, with subsequent studies extending the biology across tumour cell types and probing the mechanistic details of membrane HDM2-targeted killing.

Foundational surface HDM2 mechanism characterisation: The landmark studies establishing PNC-27’s mechanism documented that HDM2 is expressed at the plasma membrane surface of cancer cells — detectable by surface biotinylation, flow cytometry with non-permeabilised cells, and confocal microscopy — while absent from the surface of normal non-transformed cells of the same lineage. These studies established the PNC-27/surface HDM2 binding interaction by demonstrating that: PNC-27 co-localises with surface HDM2 at the cancer cell plasma membrane; neutralisation of PNC-27 with anti-p53 antibodies targeting the MDM2-binding sequence abolishes PNC-27 cytotoxicity; and HDM2 knockdown in cancer cells reduces PNC-27 sensitivity — collectively establishing surface HDM2 as the cancer cell selectivity determinant and receptor for PNC-27’s membranolytic activity.

Necrotic cell death characterisation: Studies documenting the morphological and biochemical features of PNC-27-induced cancer cell death characterised the rapid plasma membrane permeabilisation, LDH and HMGB1 release, absence of caspase-3/7 activation, and electron microscopic necrotic cell morphology — establishing necrosis as the cell death modality. The contrast with camptothecin and doxorubicin-treated cells — exhibiting apoptotic morphology, caspase activation, and PARP cleavage — established PNC-27’s necrotic killing as mechanistically distinct from conventional genotoxic anticancer agents and from intracellular MDM2 inhibitor-driven p53-dependent apoptosis.

p53-independence validation: Studies examining PNC-27 activity in p53 wild-type versus p53-null isogenic cancer cell pairs — and in cancer cells expressing dominant-negative p53 mutants — documented equivalent PNC-27 cytotoxicity regardless of p53 status, confirming that the membrane HDM2-targeted mechanism operates independently of intracellular p53 expression or transcriptional activity. These p53-independence studies established the mechanistic basis for PNC-27’s potential utility in p53-mutant cancers where conventional p53-restoring MDM2 inhibitors would be inactive.

Pancreatic cancer studies: Studies examining PNC-27 in pancreatic ductal adenocarcinoma (PDAC) cell lines — where p53 mutations are present in approximately 75% of tumours and gemcitabine resistance is frequent — documented PNC-27 cytotoxicity in PDAC cells expressing surface HDM2, with activity in both gemcitabine-sensitive and gemcitabine-resistant sublines. These pancreatic cancer studies provided the most extensive tumour type-specific characterisation of PNC-27 biology and established the pancreatic cancer context as a primary pre-clinical research model for PNC-27’s p53-independent surface HDM2-targeted mechanism.

Selectivity studies in normal versus cancer cell pairs: Studies comparing PNC-27 cytotoxicity in matched normal and cancer cell pairs — including normal melanocytes versus melanoma, normal pancreatic ductal cells versus PDAC, and normal breast epithelial cells versus breast cancer lines — documented selective killing of cancer cells at concentrations sparing normal counterparts. These selectivity studies characterised the therapeutic index of PNC-27 in paired cell systems and attributed the differential sensitivity to surface HDM2 expression — with normal cells lacking detectable surface HDM2 and therefore not providing the HDM2-dependent membrane tethering required for PNC-27’s local concentration-dependent membranolytic activity.

PNC-28 comparative studies: Studies comparing PNC-27 and PNC-28 in matched cancer cell systems characterised differences in potency, surface HDM2 binding affinity, and the structural basis of activity differences between the two N-terminal p53 domain sequences — providing the structure-activity data within the chimeric peptide family and establishing PNC-27 as the higher-potency member of the series in the cell systems examined.

PNC-27 vs Related p53/MDM2 Pathway and Anticancer Peptide Research Compounds

Compound	Class	Mechanism	MDM2 Interaction Site	p53 Dependency	Cell Death Modality	Key Research Distinction
PNC-27	Chimeric p53/penetratin peptide	Surface HDM2 binding → membrane pore formation → necrosis	Plasma membrane-resident HDM2	p53-independent	Necrosis	Membrane-targeted; cancer cell selective; p53-independent; necrotic; surface HDM2 probe
PNC-28	Chimeric p53/penetratin peptide (distinct p53 domain)	Surface HDM2 binding → membrane disruption	Plasma membrane-resident HDM2	p53-independent	Necrosis	PNC-27 family member; different N-terminal p53 sequence; SAR comparator
Nutlin-3a	Cis-imidazoline small molecule	Intracellular MDM2 hydrophobic cleft occupancy — blocks p53/MDM2 interaction	Intracellular MDM2 (nuclear/cytoplasmic)	p53-dependent (requires wild-type p53)	Apoptosis (p53-driven)	Reference intracellular MDM2 inhibitor; p53-dependent; apoptotic; mechanistic MDM2 interaction comparator
RG7112 (R7112)	Small molecule MDM2 inhibitor	Intracellular MDM2 hydrophobic cleft	Intracellular MDM2	p53-dependent	Apoptosis	Clinical-stage intracellular MDM2 inhibitor; p53-dependent comparator
ATSP-7041	Stapled p53 helix peptide	Intracellular MDM2 + MDMX dual inhibition	Intracellular MDM2/MDMX	p53-dependent	Apoptosis	Cell-permeable stapled helix; intracellular dual MDM2/MDMX; apoptotic comparator
RITA	Small molecule — binds p53 N-terminus	Allosteric p53/MDM2 disruption via p53 binding	p53 N-terminus (indirectly disrupts MDM2 binding)	p53-dependent	Apoptosis	p53-binding approach vs MDM2-binding; mechanistically distinct comparator
Penetratin (alone)	Cell-penetrating peptide	Membrane translocation — endocytosis/direct permeation	No MDM2 binding	p53-independent	Variable (concentration-dependent)	CPP control — penetratin without p53 domain; establishes MDM2-binding contribution to PNC-27 selectivity

Buying PNC-27 in Europe — What’s Included

Every order of PNC-27 dispatched to EU and European research institutions includes:

• Batch-Specific Certificate of Analysis (CoA)
• HPLC Chromatogram
• Mass Spectrometry Confirmation
• Sterility and Endotoxin Testing Reports
• Reconstitution Protocol
• Technical Research Support

Frequently Asked Questions — PNC-27 EU

Can I Buy PNC-27 in the EU and Europe?

Yes. We supply research-grade PNC-27 with fast tracked dispatch to all EU member states and wider European destinations. All orders include full batch documentation. PNC-27 is supplied strictly for laboratory research use only.

What is the Structural Design of PNC-27 and Why are Both Domains Required for Activity?

PNC-27 is a chimeric 32-amino acid peptide constructed from two fused functional domains. The N-terminal domain (residues 1–16) replicates the α-helical MDM2-binding segment of the p53 transactivation domain — specifically the p53 residues Phe¹⁹, Trp²³, and Leu²⁶ that insert into the hydrophobic cleft of MDM2 and constitute the primary p53/MDM2 interaction pharmacophore. This domain provides the selectivity determinant — binding surface HDM2 on cancer cells to tether PNC-27 at the plasma membrane. The C-terminal domain (residues 17–32) is penetratin — the Antennapedia homeodomain-derived cationic cell-penetrating peptide that, when concentrated at the membrane surface through HDM2-dependent tethering, drives membrane destabilisation and pore formation through electrostatic interaction with anionic membrane lipids and hydrophobic insertion. Neither domain alone produces the cancer cell selective membranolytic activity of the intact chimera: the p53 domain without penetratin binds MDM2 but lacks membranolytic capacity; penetratin without the p53 domain enters cells through endocytosis or non-specific membrane interaction without the HDM2-dependent surface accumulation that concentrates the peptide selectively at cancer cell membranes. The chimeric design therefore achieves selectivity through MDM2-dependent membrane tethering that locally concentrates the penetratin membranolytic sequence above the threshold required for membrane disruption — exclusively at cancer cell surfaces expressing HDM2.

Why is Surface HDM2 Expression Restricted to Cancer Cells?

The molecular basis of the cancer cell-specific membrane localisation of HDM2 is an active area of research investigation. In normal cells, HDM2 localises primarily to the nucleus and cytoplasm — where it functions as an E3 ubiquitin ligase targeting p53 for proteasomal degradation and shuttles between nucleus and cytoplasm in response to stress signals. In transformed cancer cells, aberrant HDM2 trafficking — potentially driven by oncogenic signalling, altered post-translational modification, or cancer cell-specific membrane lipid composition changes — produces a fraction of HDM2 protein at the plasma membrane outer leaflet or accessible surface. The precise mechanisms governing this differential membrane localisation in cancer versus normal cells — including the role of specific HDM2 post-translational modifications, oncogene-driven trafficking alterations, and plasma membrane composition differences between normal and malignant cells — constitute a research question that PNC-27 itself serves as a probe to investigate.

How Does PNC-27 Differ From Nutlin-3a as a Research Tool for MDM2 Biology?

Nutlin-3a and PNC-27 both target MDM2 through the p53 transactivation domain binding interface but engage fundamentally different pools of MDM2 in distinct cellular compartments. Nutlin-3a is a cell-permeable small molecule that penetrates into the cell and occupies the hydrophobic cleft of intracellular nuclear and cytoplasmic MDM2 — preventing MDM2 from binding and ubiquitinating p53, thereby stabilising and activating p53 and driving p53-dependent apoptotic transcriptional programmes. This mechanism requires wild-type, transcriptionally competent p53 — making Nutlin-3a inactive in p53-null or p53-mutant cancer cells. PNC-27 targets surface membrane-resident HDM2 — producing membrane disruption and p53-independent necrotic killing regardless of intracellular p53 status. For research, this distinction enables mechanistic dissection of surface versus intracellular MDM2 biology, allows the contributions of each MDM2 pool to cancer cell biology to be studied independently, and establishes PNC-27 as the tool for studying surface HDM2 — a biological phenomenon inaccessible to intracellular MDM2 inhibitors.

Is PNC-27 Active Against Multidrug-Resistant Cancer Cells?

Because PNC-27’s mechanism of cancer cell killing — surface HDM2 binding followed by plasma membrane pore formation and necrotic death — is independent of the intracellular drug efflux pumps (P-glycoprotein/MDR1, MRP1, BCRP) that drive multidrug resistance to conventional chemotherapy, and does not require functional intracellular apoptosis pathways (caspases, Bcl-2 family, p53) that are frequently dysregulated in drug-resistant cancer cells, PNC-27 has been examined in drug-resistant cancer cell models as a mechanistic complement to conventional chemotherapy. Studies in gemcitabine-resistant pancreatic cancer cells and doxorubicin-resistant cancer lines have documented PNC-27 cytotoxicity in drug-resistant sublines — with sensitivity correlating with surface HDM2 expression rather than with the drug resistance mechanisms that determine conventional chemotherapy sensitivity.

What Controls are Required for Mechanistic PNC-27 Research?

Rigorous mechanistic interpretation of PNC-27 experiments requires several key controls. Penetratin-only controls (the C-terminal domain without the p53 N-terminal sequence) establish the baseline cytotoxicity of the CPP domain and confirm that the HDM2-binding N-terminal domain is required for cancer cell selectivity. Scrambled PNC-27 controls (randomised amino acid sequence with identical composition) confirm sequence specificity of the observed cytotoxicity. MDM2/HDM2 siRNA knockdown in cancer cell lines — reducing surface HDM2 expression — should attenuate PNC-27 sensitivity proportionally. Anti-MDM2 antibody pre-treatment that blocks surface HDM2 should similarly reduce PNC-27 binding and cytotoxicity. Caspase inhibitor (z-VAD-FMK) controls confirm caspase-independence of PNC-27-driven cell death. Parallel treatment of matched normal and cancer cell pairs from the same tissue lineage establishes the cancer cell selectivity that is the defining pharmacological property of PNC-27.

How Do I Reconstitute PNC-27 for Laboratory Use?

Reconstitute with sterile water or PBS by adding solvent slowly down the vial wall and swirling gently — do not vortex. PNC-27 is a 32-amino acid cationic peptide containing the arginine-rich penetratin sequence that may exhibit concentration-dependent self-aggregation at high stock concentrations — prepare initial stocks at moderate concentration (1–5 mM) in sterile water or PBS and dilute to working concentrations (typically 10–100 μM for cancer cell cytotoxicity studies) in serum-free or low-serum cell culture medium immediately before use, as serum proteins can bind the cationic penetratin domain and reduce effective peptide concentration. Aliquot into single-use volumes and store at -80°C to avoid repeated freeze-thaw degradation. Verify reconstitution completeness visually and, for quantitative experiments, spectrophotometrically using PNC-27’s tryptophan absorbance at 280 nm.

How Quickly is PNC-27 Delivered to Europe?

Delivery to EU and European destinations typically takes 3–7 working days via tracked international courier with packaging maintaining peptide stability throughout transit.

Product Specifications

Parameter	Detail
Peptide	PNC-27
Length	32 amino acids
Architecture	Chimeric peptide — N-terminal p53 transactivation domain (MDM2-binding) + C-terminal penetratin (CPP)
N-terminal Domain	p53 transactivation domain residues 12–26 — MDM2 hydrophobic cleft binding pharmacophore (Phe¹⁹, Trp²³, Leu²⁶)
C-terminal Domain	Penetratin (Antennapedia homeodomain CPP) — membrane-active, membranolytic at local high concentration
Primary Target	Plasma membrane-resident HDM2 (surface MDM2) — cancer cell selective
Mechanism	Surface HDM2 binding → local peptide accumulation → membrane pore formation → necrotic cell death
p53 Dependency	None — p53-independent (kills p53-null and p53-mutant cancer cells)
Cell Death Modality	Necrosis — rapid membrane permeabilisation; caspase-independent; LDH/HMGB1 release
Cancer Cell Selectivity	Surface HDM2 expression — absent from normal non-transformed cells
Related Compound	PNC-28 — related chimeric peptide with distinct N-terminal p53 domain sequence
Primary Research Interest	Surface HDM2 biology, cancer cell selective cytotoxicity, p53-independent cancer killing, necrotic cell death, membrane-active anticancer peptide pharmacology, MDM2 comparative biology
Purity	≥99%
Verification	HPLC & Mass Spectrometry
Form	Sterile Lyophilised Powder
Solubility	Sterile water or PBS (low-serum medium for cell treatment; avoid high serum concentrations)
Storage	-20°C, protected from light and moisture
Intended Use	Research use only

Research Disclaimer

PNC-27 is supplied exclusively for legitimate scientific research conducted within licensed laboratory environments. This product is not approved for human consumption, self-administration, or any therapeutic, clinical, or veterinary application. It must be handled solely by qualified researchers in compliance with applicable EU regulations, national legislation, and institutional ethics guidelines. By purchasing, you confirm this compound will be used exclusively for approved in vitro or pre-clinical research purposes.